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Database: UniProt
Entry: V7B5U8_PHAVU
LinkDB: V7B5U8_PHAVU
Original site: V7B5U8_PHAVU 
ID   V7B5U8_PHAVU            Unreviewed;       478 AA.
AC   V7B5U8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=monodehydroascorbate reductase (NADH) {ECO:0000256|ARBA:ARBA00038920};
DE            EC=1.6.5.4 {ECO:0000256|ARBA:ARBA00038920};
GN   ORFNames=PHAVU_008G155600g {ECO:0000313|EMBL:ESW12955.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW12955.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 monodehydro-L-ascorbate radical + NADH = 2 L-
CC         ascorbate + NAD(+); Xref=Rhea:RHEA:14581, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:38290, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:59513; EC=1.6.5.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036831};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00006442}.
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DR   EMBL; CM002295; ESW12955.1; -; Genomic_DNA.
DR   RefSeq; XP_007140961.1; XM_007140899.1.
DR   AlphaFoldDB; V7B5U8; -.
DR   STRING; 3885.V7B5U8; -.
DR   EnsemblPlants; ESW12955; ESW12955; PHAVU_008G155600g.
DR   GeneID; 18622995; -.
DR   Gramene; ESW12955; ESW12955; PHAVU_008G155600g.
DR   KEGG; pvu:PHAVU_008G155600g; -.
DR   eggNOG; KOG1336; Eukaryota.
DR   OMA; VANHHNG; -.
DR   OrthoDB; 804at2759; -.
DR   PhylomeDB; V7B5U8; -.
DR   Proteomes; UP000000226; Chromosome 8.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:EnsemblPlants.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IEA:EnsemblPlants.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:EnsemblPlants.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR048618; MDHAR3-like_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF21791; MDHAR3-like_C; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        449..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..321
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          340..423
FT                   /note="Monodehydroascorbate reductase 3-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21791"
SQ   SEQUENCE   478 AA;  52064 MW;  98B7918247B5DCF4 CRC64;
     MGRAFVYVIL GGGVAAGYAA LEFVKKGVSY GELCIISDEP VAPYERPALS KGFLLPEAAA
     RLPSFHTCVG ANEERLTPKW YKEHGIELVL GTGVKSADVK RKTLLTTTGE TISYKFLIVA
     TGARALKLEE FGVSGSDAEN VCYLRDIADA NRLVNVIQSC PEGNAVVIGG GYIGMECAAS
     LVINKINVTM VFPEEHCMAR LFTTKIANYY EEYYKSRGVN FVKGTVMSSF DFDSNGKVTA
     VNLRDGSTLS VEMVVVGIGI RPNTGLFEGQ LTLEKGGIKV NGMLQSSNSS VYAIGDVAAF
     PVKAFGETRR LEHVDSARKS AKHVVAAIME PDKTGEFDYL PFFYSRIFTL SWQFYGDNVG
     EVIYYGDMSG SAFGAYWVSK GHLVGAFLEG GNREEYEAIA KVTRLRPAIE DLTELERQGL
     GYAVTVSQKP VASPAVEVRA SDLLLEKPLY AWHATAGVII AASIAAFAYF YGKKRRRW
//
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